A bacteriophage tubulin homolog, PhuZ, forms a structure with the biochemical, structural, and functional properties of a simplified, bipolar spindle.

Neuronal networks balance flexibility with stability by allowing the firing rate of individual neurons within a network to vary over time, while ensuring that the average firing rate across the network remains constant.

Single-molecule imaging of CTCF and cohesin in live cells suggests that chromatin loops are dynamic structures that frequently form and fall apart.

A fast evolutionary approach to engineer membrane protein kinetic stability yields folded excitatory neurotransmitter transporters and provides insights into their denaturing pathway.

A combination of cryo-electron microscopy of TPX2 bound to microtubules and in vitro reconstitution experiments reveals a novel microtubule interaction mode that explains how TPX2 promotes microtubule nucleation and stabilization.

The EB binding region defines the length of the protective cap that stabilizes growing microtubules.

Crowding and metabolites in a simulated cellular environment alter protein conformations, modulate interactions of functionally related proteins, and lead to significant dynamic heterogeneity.

A new combined mechanism explains how GTP binding by tubulin is linked to its dynamics and energetics in solution and why GTP-induced flexibility, and not the tubulin conformation as such, drives microtubule assembly.

Axonal arborisation growth is regulated by dynamic, focal localisations of Neurexin and Neuroligin that provide stability for filopodia, enabling a 'stick and grow'-based mechanism, wholly independent of synapse formation.